HEADER OXIDOREDUCTASE 13-DEC-99 1DM7
TITLE BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH
TITLE 2 HOMOARGININE (H4B FREE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HEME DOMAIN;
COMPND 5 EC: 1.14.13.39;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 CELL: ENDOTHELIAL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA-BETA FOLD, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.S.RAMAN,H.LI,P.MARTASEK,G.J.SOUTHAN,B.S.S.MASTERS,T.L.POULOS
REVDAT 4 07-FEB-24 1DM7 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 1DM7 1 VERSN
REVDAT 2 24-FEB-09 1DM7 1 VERSN
REVDAT 1 13-DEC-00 1DM7 0
JRNL AUTH C.S.RAMAN,H.LI,P.MARTASEK,G.J.SOUTHAN,B.S.S.MASTERS,
JRNL AUTH 2 T.L.POULOS
JRNL TITL CRYSTAL STRUCTURES OF BOVINE ENDOTHELIAL NITRIC OXIDE
JRNL TITL 2 SYNTHASE HEME DOMAIN COMPLEXED WITH VARIOUS INHIBITORS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.S.RAMAN,H.LI,P.MARTASEK,V.KRAL,B.S.S.MASTERS,T.L.POULOS
REMARK 1 TITL CRYSTAL STRUCTURE OF CONSTITUTIVE ENDOTHELIAL NITRIC OXIDE
REMARK 1 TITL 2 SYNTHASE: A PARADIGM FOR PTERIN FUNCTION INVOLVING A NOVEL
REMARK 1 TITL 3 METAL CENTER
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 95 939 1998
REMARK 1 REFN ISSN 0092-8674
REMARK 1 DOI 10.1016/S0092-8674(00)81718-3
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.R.CRANE,A.S.ARVAI,D.K.GHOSH,C.WU,E.D.GETZOFF,D.J.STUEHR,
REMARK 1 AUTH 2 A.TAINER
REMARK 1 TITL STRUCTURE OF NITRIC OXIDE SYNTHASE OXYGENASE DIMER WITH
REMARK 1 TITL 2 PTERIN AND SUBSTRATE
REMARK 1 REF SCIENCE V. 279 2121 1998
REMARK 1 REFN ISSN 0036-8075
REMARK 1 DOI 10.1126/SCIENCE.279.5359.2121
REMARK 1 REFERENCE 3
REMARK 1 AUTH A.RENODON-CORNIERE,J.-L.BOUCHER,S.DIJOLS,D.J.STUEHR,D.MANSUY
REMARK 1 TITL EFFICIENT FORMATION OF NITRIC OXIDE FROM SELECTIVE OXIDATION
REMARK 1 TITL 2 OF N-ARYL N'- HYDROXYGUANIDINES BY INDUCIBLE NITRIC OXIDE
REMARK 1 TITL 3 SYNTHASE
REMARK 1 REF BIOCHEMISTRY V. 38 4663 1999
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI982930P
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2579569.550
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 57223
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2837
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.18
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5192
REMARK 3 BIN R VALUE (WORKING SET) : 0.4320
REMARK 3 BIN FREE R VALUE : 0.4250
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 285
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.025
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6593
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 157
REMARK 3 SOLVENT ATOMS : 409
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 24.31000
REMARK 3 B22 (A**2) : -13.00000
REMARK 3 B33 (A**2) : -11.31000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.59
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.61
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.010
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 54.80
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 RESIDUES 39 TO 66 OF MOLECULE A AND RESIDUES 39 TO 68 IN
REMARK 3 MOLECULE B ARE NOT VISIBLE IN THE ELECTRON DENSITY.
REMARK 3
REMARK 3 RESIDUES 108-120 ARE DISORDERED, BUT THE TENTATIVE MODEL
REMARK 3 WAS INCLUDED IN THE REFINEMENT.
REMARK 4
REMARK 4 1DM7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-99.
REMARK 100 THE DEPOSITION ID IS D_1000010205.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66766
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.47000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, CACODYLATE, MAGNESIUM
REMARK 280 ACETATE, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 280K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 29.48000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.30000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.99500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.30000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.48000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.99500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 39
REMARK 465 ARG A 40
REMARK 465 ALA A 41
REMARK 465 PRO A 42
REMARK 465 ALA A 43
REMARK 465 PRO A 44
REMARK 465 ALA A 45
REMARK 465 THR A 46
REMARK 465 PRO A 47
REMARK 465 HIS A 48
REMARK 465 ALA A 49
REMARK 465 PRO A 50
REMARK 465 ASP A 51
REMARK 465 HIS A 52
REMARK 465 SER A 53
REMARK 465 PRO A 54
REMARK 465 ALA A 55
REMARK 465 PRO A 56
REMARK 465 ASN A 57
REMARK 465 SER A 58
REMARK 465 PRO A 59
REMARK 465 THR A 60
REMARK 465 LEU A 61
REMARK 465 THR A 62
REMARK 465 ARG A 63
REMARK 465 PRO A 64
REMARK 465 PRO A 65
REMARK 465 GLU A 66
REMARK 465 SER B 39
REMARK 465 ARG B 40
REMARK 465 ALA B 41
REMARK 465 PRO B 42
REMARK 465 ALA B 43
REMARK 465 PRO B 44
REMARK 465 ALA B 45
REMARK 465 THR B 46
REMARK 465 PRO B 47
REMARK 465 HIS B 48
REMARK 465 ALA B 49
REMARK 465 PRO B 50
REMARK 465 ASP B 51
REMARK 465 HIS B 52
REMARK 465 SER B 53
REMARK 465 PRO B 54
REMARK 465 ALA B 55
REMARK 465 PRO B 56
REMARK 465 ASN B 57
REMARK 465 SER B 58
REMARK 465 PRO B 59
REMARK 465 THR B 60
REMARK 465 LEU B 61
REMARK 465 THR B 62
REMARK 465 ARG B 63
REMARK 465 PRO B 64
REMARK 465 PRO B 65
REMARK 465 GLU B 66
REMARK 465 GLY B 67
REMARK 465 PRO B 68
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLN B 258 CB - CA - C ANGL. DEV. = 15.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 69 43.21 -94.20
REMARK 500 ARG A 109 89.99 -63.67
REMARK 500 LYS A 110 -75.04 -142.37
REMARK 500 GLN A 112 105.19 -17.02
REMARK 500 SER A 116 51.17 -114.66
REMARK 500 PRO A 117 -63.87 -26.21
REMARK 500 PRO A 119 142.58 -34.73
REMARK 500 ARG A 142 19.94 -141.62
REMARK 500 LYS A 194 78.43 -115.08
REMARK 500 ASP A 260 -7.96 -59.21
REMARK 500 ASN A 285 32.52 -155.03
REMARK 500 PRO A 308 107.48 -53.83
REMARK 500 PRO A 309 -39.64 -36.65
REMARK 500 ALA A 353 64.03 -165.18
REMARK 500 ARG A 374 -137.86 -122.79
REMARK 500 PRO A 473 154.82 -45.91
REMARK 500 LEU B 111 20.28 -69.96
REMARK 500 GLN B 112 -158.01 -57.18
REMARK 500 THR B 113 59.19 -140.16
REMARK 500 ARG B 114 152.77 -34.39
REMARK 500 PRO B 115 167.20 -37.47
REMARK 500 PRO B 121 109.89 -34.88
REMARK 500 ARG B 142 31.87 -141.62
REMARK 500 SER B 145 -177.69 -62.08
REMARK 500 ASP B 202 58.62 -92.35
REMARK 500 GLN B 258 -152.11 -65.82
REMARK 500 ASN B 285 24.60 -148.83
REMARK 500 PRO B 298 138.02 -39.47
REMARK 500 ASP B 299 32.86 38.07
REMARK 500 THR B 366 -61.64 -102.34
REMARK 500 ARG B 374 -144.18 -116.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 ZN ION SITS RIGHT ON THE NCS 2-FOLD THAT DEFINES THE DIMER
REMARK 600 INTERFACE AND IS COORDINATED TETRAHEDRALLY WITH 2 PAIRS OF
REMARK 600 SYMMETRY-RELATED CYS RESIDUES.
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B2900 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 96 SG
REMARK 620 2 CYS A 101 SG 109.9
REMARK 620 3 CYS B 96 SG 115.1 106.4
REMARK 620 4 CYS B 101 SG 105.2 103.7 115.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A1500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 186 SG
REMARK 620 2 HEM A1500 NA 100.2
REMARK 620 3 HEM A1500 NB 92.1 88.8
REMARK 620 4 HEM A1500 NC 101.5 158.3 90.2
REMARK 620 5 HEM A1500 ND 100.9 90.5 166.9 85.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CAC A 950 AS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 384 SG
REMARK 620 2 CAC A 950 C1 97.0
REMARK 620 3 CAC A 950 C2 94.9 94.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B2500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 186 SG
REMARK 620 2 HEM B2500 NA 99.5
REMARK 620 3 HEM B2500 NB 94.9 88.7
REMARK 620 4 HEM B2500 NC 95.5 165.0 89.9
REMARK 620 5 HEM B2500 ND 95.5 91.3 169.4 87.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CAC B 950 AS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 384 SG
REMARK 620 2 CAC B 950 C1 95.0
REMARK 620 3 CAC B 950 C2 96.2 94.2
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1860
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC A 950
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 2860
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC B 950
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 2500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HRG A 1740
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HRG B 2740
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1885
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1890
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2880
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 2885
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 2890
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NSE RELATED DB: PDB
REMARK 900 BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH
REMARK 900 L-ARGININE
DBREF 1DM7 A 39 482 UNP P29473 NOS3_BOVIN 39 482
DBREF 1DM7 B 39 482 UNP P29473 NOS3_BOVIN 39 482
SEQADV 1DM7 ARG A 100 UNP P29473 CYS 100 CONFLICT
SEQADV 1DM7 ARG B 100 UNP P29473 CYS 100 CONFLICT
SEQRES 1 A 444 SER ARG ALA PRO ALA PRO ALA THR PRO HIS ALA PRO ASP
SEQRES 2 A 444 HIS SER PRO ALA PRO ASN SER PRO THR LEU THR ARG PRO
SEQRES 3 A 444 PRO GLU GLY PRO LYS PHE PRO ARG VAL LYS ASN TRP GLU
SEQRES 4 A 444 LEU GLY SER ILE THR TYR ASP THR LEU CYS ALA GLN SER
SEQRES 5 A 444 GLN GLN ASP GLY PRO CYS THR PRO ARG ARG CYS LEU GLY
SEQRES 6 A 444 SER LEU VAL LEU PRO ARG LYS LEU GLN THR ARG PRO SER
SEQRES 7 A 444 PRO GLY PRO PRO PRO ALA GLU GLN LEU LEU SER GLN ALA
SEQRES 8 A 444 ARG ASP PHE ILE ASN GLN TYR TYR SER SER ILE LYS ARG
SEQRES 9 A 444 SER GLY SER GLN ALA HIS GLU GLU ARG LEU GLN GLU VAL
SEQRES 10 A 444 GLU ALA GLU VAL ALA SER THR GLY THR TYR HIS LEU ARG
SEQRES 11 A 444 GLU SER GLU LEU VAL PHE GLY ALA LYS GLN ALA TRP ARG
SEQRES 12 A 444 ASN ALA PRO ARG CYS VAL GLY ARG ILE GLN TRP GLY LYS
SEQRES 13 A 444 LEU GLN VAL PHE ASP ALA ARG ASP CYS SER SER ALA GLN
SEQRES 14 A 444 GLU MET PHE THR TYR ILE CYS ASN HIS ILE LYS TYR ALA
SEQRES 15 A 444 THR ASN ARG GLY ASN LEU ARG SER ALA ILE THR VAL PHE
SEQRES 16 A 444 PRO GLN ARG ALA PRO GLY ARG GLY ASP PHE ARG ILE TRP
SEQRES 17 A 444 ASN SER GLN LEU VAL ARG TYR ALA GLY TYR ARG GLN GLN
SEQRES 18 A 444 ASP GLY SER VAL ARG GLY ASP PRO ALA ASN VAL GLU ILE
SEQRES 19 A 444 THR GLU LEU CYS ILE GLN HIS GLY TRP THR PRO GLY ASN
SEQRES 20 A 444 GLY ARG PHE ASP VAL LEU PRO LEU LEU LEU GLN ALA PRO
SEQRES 21 A 444 ASP GLU ALA PRO GLU LEU PHE VAL LEU PRO PRO GLU LEU
SEQRES 22 A 444 VAL LEU GLU VAL PRO LEU GLU HIS PRO THR LEU GLU TRP
SEQRES 23 A 444 PHE ALA ALA LEU GLY LEU ARG TRP TYR ALA LEU PRO ALA
SEQRES 24 A 444 VAL SER ASN MET LEU LEU GLU ILE GLY GLY LEU GLU PHE
SEQRES 25 A 444 SER ALA ALA PRO PHE SER GLY TRP TYR MET SER THR GLU
SEQRES 26 A 444 ILE GLY THR ARG ASN LEU CYS ASP PRO HIS ARG TYR ASN
SEQRES 27 A 444 ILE LEU GLU ASP VAL ALA VAL CYS MET ASP LEU ASP THR
SEQRES 28 A 444 ARG THR THR SER SER LEU TRP LYS ASP LYS ALA ALA VAL
SEQRES 29 A 444 GLU ILE ASN LEU ALA VAL LEU HIS SER PHE GLN LEU ALA
SEQRES 30 A 444 LYS VAL THR ILE VAL ASP HIS HIS ALA ALA THR VAL SER
SEQRES 31 A 444 PHE MET LYS HIS LEU ASP ASN GLU GLN LYS ALA ARG GLY
SEQRES 32 A 444 GLY CYS PRO ALA ASP TRP ALA TRP ILE VAL PRO PRO ILE
SEQRES 33 A 444 SER GLY SER LEU THR PRO VAL PHE HIS GLN GLU MET VAL
SEQRES 34 A 444 ASN TYR ILE LEU SER PRO ALA PHE ARG TYR GLN PRO ASP
SEQRES 35 A 444 PRO TRP
SEQRES 1 B 444 SER ARG ALA PRO ALA PRO ALA THR PRO HIS ALA PRO ASP
SEQRES 2 B 444 HIS SER PRO ALA PRO ASN SER PRO THR LEU THR ARG PRO
SEQRES 3 B 444 PRO GLU GLY PRO LYS PHE PRO ARG VAL LYS ASN TRP GLU
SEQRES 4 B 444 LEU GLY SER ILE THR TYR ASP THR LEU CYS ALA GLN SER
SEQRES 5 B 444 GLN GLN ASP GLY PRO CYS THR PRO ARG ARG CYS LEU GLY
SEQRES 6 B 444 SER LEU VAL LEU PRO ARG LYS LEU GLN THR ARG PRO SER
SEQRES 7 B 444 PRO GLY PRO PRO PRO ALA GLU GLN LEU LEU SER GLN ALA
SEQRES 8 B 444 ARG ASP PHE ILE ASN GLN TYR TYR SER SER ILE LYS ARG
SEQRES 9 B 444 SER GLY SER GLN ALA HIS GLU GLU ARG LEU GLN GLU VAL
SEQRES 10 B 444 GLU ALA GLU VAL ALA SER THR GLY THR TYR HIS LEU ARG
SEQRES 11 B 444 GLU SER GLU LEU VAL PHE GLY ALA LYS GLN ALA TRP ARG
SEQRES 12 B 444 ASN ALA PRO ARG CYS VAL GLY ARG ILE GLN TRP GLY LYS
SEQRES 13 B 444 LEU GLN VAL PHE ASP ALA ARG ASP CYS SER SER ALA GLN
SEQRES 14 B 444 GLU MET PHE THR TYR ILE CYS ASN HIS ILE LYS TYR ALA
SEQRES 15 B 444 THR ASN ARG GLY ASN LEU ARG SER ALA ILE THR VAL PHE
SEQRES 16 B 444 PRO GLN ARG ALA PRO GLY ARG GLY ASP PHE ARG ILE TRP
SEQRES 17 B 444 ASN SER GLN LEU VAL ARG TYR ALA GLY TYR ARG GLN GLN
SEQRES 18 B 444 ASP GLY SER VAL ARG GLY ASP PRO ALA ASN VAL GLU ILE
SEQRES 19 B 444 THR GLU LEU CYS ILE GLN HIS GLY TRP THR PRO GLY ASN
SEQRES 20 B 444 GLY ARG PHE ASP VAL LEU PRO LEU LEU LEU GLN ALA PRO
SEQRES 21 B 444 ASP GLU ALA PRO GLU LEU PHE VAL LEU PRO PRO GLU LEU
SEQRES 22 B 444 VAL LEU GLU VAL PRO LEU GLU HIS PRO THR LEU GLU TRP
SEQRES 23 B 444 PHE ALA ALA LEU GLY LEU ARG TRP TYR ALA LEU PRO ALA
SEQRES 24 B 444 VAL SER ASN MET LEU LEU GLU ILE GLY GLY LEU GLU PHE
SEQRES 25 B 444 SER ALA ALA PRO PHE SER GLY TRP TYR MET SER THR GLU
SEQRES 26 B 444 ILE GLY THR ARG ASN LEU CYS ASP PRO HIS ARG TYR ASN
SEQRES 27 B 444 ILE LEU GLU ASP VAL ALA VAL CYS MET ASP LEU ASP THR
SEQRES 28 B 444 ARG THR THR SER SER LEU TRP LYS ASP LYS ALA ALA VAL
SEQRES 29 B 444 GLU ILE ASN LEU ALA VAL LEU HIS SER PHE GLN LEU ALA
SEQRES 30 B 444 LYS VAL THR ILE VAL ASP HIS HIS ALA ALA THR VAL SER
SEQRES 31 B 444 PHE MET LYS HIS LEU ASP ASN GLU GLN LYS ALA ARG GLY
SEQRES 32 B 444 GLY CYS PRO ALA ASP TRP ALA TRP ILE VAL PRO PRO ILE
SEQRES 33 B 444 SER GLY SER LEU THR PRO VAL PHE HIS GLN GLU MET VAL
SEQRES 34 B 444 ASN TYR ILE LEU SER PRO ALA PHE ARG TYR GLN PRO ASP
SEQRES 35 B 444 PRO TRP
HET ACT A1860 4
HET CAC A 950 3
HET HEM A1500 43
HET HRG A1740 13
HET GOL A1885 6
HET GOL A1890 6
HET GOL A2880 6
HET ACT B2860 4
HET CAC B 950 3
HET ZN B2900 1
HET HEM B2500 43
HET HRG B2740 13
HET GOL B2885 6
HET GOL B2890 6
HETNAM ACT ACETATE ION
HETNAM CAC CACODYLATE ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM HRG L-HOMOARGININE
HETNAM GOL GLYCEROL
HETNAM ZN ZINC ION
HETSYN CAC DIMETHYLARSINATE
HETSYN HEM HEME
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 4 CAC 2(C2 H6 AS O2 1-)
FORMUL 5 HEM 2(C34 H32 FE N4 O4)
FORMUL 6 HRG 2(C7 H16 N4 O2)
FORMUL 7 GOL 5(C3 H8 O3)
FORMUL 12 ZN ZN 2+
FORMUL 17 HOH *409(H2 O)
HELIX 1 1 THR A 85 SER A 90 5 6
HELIX 2 2 PRO A 121 ILE A 140 1 20
HELIX 3 3 SER A 145 GLY A 163 1 19
HELIX 4 4 ARG A 168 ALA A 183 1 16
HELIX 5 5 GLY A 188 TRP A 192 5 5
HELIX 6 6 SER A 205 ASN A 222 1 18
HELIX 7 7 ARG A 223 ASN A 225 5 3
HELIX 8 8 ASN A 269 GLN A 278 1 10
HELIX 9 9 TRP A 324 GLY A 329 5 6
HELIX 10 10 MET A 360 THR A 366 1 7
HELIX 11 11 ILE A 377 MET A 385 1 9
HELIX 12 12 THR A 391 SER A 394 5 4
HELIX 13 13 LEU A 395 ALA A 415 1 21
HELIX 14 14 ASP A 421 GLY A 441 1 21
HELIX 15 15 ASP A 446 VAL A 451 1 6
HELIX 16 16 SER A 455 THR A 459 5 5
HELIX 17 17 THR A 459 HIS A 463 5 5
HELIX 18 18 THR B 85 SER B 90 5 6
HELIX 19 19 PRO B 121 ILE B 140 1 20
HELIX 20 20 SER B 145 GLY B 163 1 19
HELIX 21 21 ARG B 168 ALA B 183 1 16
HELIX 22 22 GLY B 188 TRP B 192 5 5
HELIX 23 23 SER B 205 ASN B 222 1 18
HELIX 24 24 ARG B 223 ASN B 225 5 3
HELIX 25 25 ASN B 269 GLN B 278 1 10
HELIX 26 26 PRO B 308 VAL B 312 5 5
HELIX 27 27 TRP B 324 GLY B 329 5 6
HELIX 28 28 SER B 361 THR B 366 1 6
HELIX 29 29 THR B 366 ASP B 371 1 6
HELIX 30 30 ILE B 377 MET B 385 1 9
HELIX 31 31 LEU B 395 ALA B 415 1 21
HELIX 32 32 ASP B 421 GLY B 441 1 21
HELIX 33 33 ASP B 446 VAL B 451 1 6
HELIX 34 34 SER B 455 THR B 459 5 5
SHEET 1 A 2 ARG A 72 LYS A 74 0
SHEET 2 A 2 ILE A 81 TYR A 83 -1 O THR A 82 N VAL A 73
SHEET 1 B 4 GLN A 196 ASP A 199 0
SHEET 2 B 4 ALA A 229 VAL A 232 1 O ILE A 230 N PHE A 198
SHEET 3 B 4 PHE A 355 SER A 356 -1 N SER A 356 O ALA A 229
SHEET 4 B 4 ALA A 337 VAL A 338 -1 O VAL A 338 N PHE A 355
SHEET 1 C 3 ARG A 244 ILE A 245 0
SHEET 2 C 3 LEU A 293 GLN A 296 -1 N GLN A 296 O ARG A 244
SHEET 3 C 3 GLU A 303 PHE A 305 -1 N GLU A 303 O LEU A 295
SHEET 1 D 2 GLY A 255 ARG A 257 0
SHEET 2 D 2 VAL A 263 GLY A 265 -1 O ARG A 264 N TYR A 256
SHEET 1 E 2 GLU A 314 PRO A 316 0
SHEET 2 E 2 ARG A 331 TYR A 333 -1 O TRP A 332 N VAL A 315
SHEET 1 F 3 LEU A 348 PHE A 350 0
SHEET 2 F 3 LEU A 342 ILE A 345 -1 O LEU A 343 N PHE A 350
SHEET 3 F 3 ALA A 474 ARG A 476 -1 O ALA A 474 N GLU A 344
SHEET 1 G 2 ARG B 72 ASN B 75 0
SHEET 2 G 2 SER B 80 TYR B 83 -1 O SER B 80 N ASN B 75
SHEET 1 H 4 GLN B 196 ASP B 199 0
SHEET 2 H 4 ALA B 229 VAL B 232 1 O ILE B 230 N PHE B 198
SHEET 3 H 4 PHE B 355 SER B 356 -1 N SER B 356 O ALA B 229
SHEET 4 H 4 ALA B 337 VAL B 338 -1 O VAL B 338 N PHE B 355
SHEET 1 I 3 ARG B 244 ILE B 245 0
SHEET 2 I 3 LEU B 293 GLN B 296 -1 N GLN B 296 O ARG B 244
SHEET 3 I 3 GLU B 303 PHE B 305 -1 N GLU B 303 O LEU B 295
SHEET 1 J 2 GLY B 255 ARG B 257 0
SHEET 2 J 2 VAL B 263 GLY B 265 -1 O ARG B 264 N TYR B 256
SHEET 1 K 2 GLU B 314 PRO B 316 0
SHEET 2 K 2 ARG B 331 TYR B 333 -1 O TRP B 332 N VAL B 315
SHEET 1 L 3 LEU B 348 PHE B 350 0
SHEET 2 L 3 MET B 341 ILE B 345 -1 O LEU B 343 N PHE B 350
SHEET 3 L 3 ALA B 474 TYR B 477 -1 O ALA B 474 N GLU B 344
SHEET 1 M 2 TYR B 359 MET B 360 0
SHEET 2 M 2 ILE B 419 VAL B 420 1 N VAL B 420 O TYR B 359
LINK SG CYS A 96 ZN ZN B2900 1555 1555 2.33
LINK SG CYS A 101 ZN ZN B2900 1555 1555 2.33
LINK SG CYS A 186 FE HEM A1500 1555 1555 2.31
LINK SG CYS A 384 AS CAC A 950 1555 1555 2.30
LINK SG CYS B 96 ZN ZN B2900 1555 1555 2.31
LINK SG CYS B 101 ZN ZN B2900 1555 1555 2.33
LINK SG CYS B 186 FE HEM B2500 1555 1555 2.27
LINK SG CYS B 384 AS CAC B 950 1555 1555 2.40
CISPEP 1 SER A 472 PRO A 473 0 0.15
CISPEP 2 SER B 472 PRO B 473 0 1.18
SITE 1 AC1 7 GLY A 188 TRP A 358 VAL A 420 SER A 428
SITE 2 AC1 7 HOH A3054 HOH A3087 HOH A3099
SITE 1 AC2 6 TRP A 324 CYS A 384 LYS A 438 ARG A 440
SITE 2 AC2 6 GLY A 441 HOH A3021
SITE 1 AC3 5 TRP B 358 VAL B 420 SER B 428 HOH B2901
SITE 2 AC3 5 HOH B2932
SITE 1 AC4 3 TYR B 83 TRP B 324 CYS B 384
SITE 1 AC5 4 CYS A 96 CYS A 101 CYS B 96 CYS B 101
SITE 1 AC6 17 TRP A 180 ARG A 185 CYS A 186 SER A 228
SITE 2 AC6 17 PHE A 355 SER A 356 TRP A 358 GLU A 363
SITE 3 AC6 17 TRP A 449 TYR A 477 HRG A1740 GOL A1890
SITE 4 AC6 17 HOH A2927 HOH A2933 HOH A2995 HOH A3020
SITE 5 AC6 17 HOH A3098
SITE 1 AC7 17 TRP B 180 ARG B 185 CYS B 186 VAL B 187
SITE 2 AC7 17 SER B 228 MET B 341 PHE B 355 SER B 356
SITE 3 AC7 17 TRP B 358 GLU B 363 TRP B 449 TYR B 477
SITE 4 AC7 17 HRG B2740 GOL B2890 HOH B2921 HOH B2923
SITE 5 AC7 17 HOH B3055
SITE 1 AC8 8 GLN A 249 TRP A 358 TYR A 359 GLU A 363
SITE 2 AC8 8 ASN A 368 HEM A1500 HOH A2986 HOH A3023
SITE 1 AC9 10 GLN B 249 TYR B 333 VAL B 338 TRP B 358
SITE 2 AC9 10 TYR B 359 GLU B 363 ASN B 368 HEM B2500
SITE 3 AC9 10 HOH B2909 HOH B3070
SITE 1 BC1 6 VAL A 263 ARG A 264 GLY A 265 ARG A 287
SITE 2 BC1 6 ARG A 374 TYR A 375
SITE 1 BC2 8 ARG A 367 ALA A 448 TRP A 449 HEM A1500
SITE 2 BC2 8 HOH A2924 HOH A2947 TRP B 447 PHE B 462
SITE 1 BC3 5 PHE A 462 GLU A 465 HOH A2903 SER B 104
SITE 2 BC3 5 GOL B2890
SITE 1 BC4 6 VAL B 263 ARG B 264 GLY B 265 PRO B 267
SITE 2 BC4 6 ARG B 287 TYR B 375
SITE 1 BC5 5 GOL A2880 ARG B 367 ALA B 448 TRP B 449
SITE 2 BC5 5 HEM B2500
CRYST1 58.960 105.990 156.600 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.016961 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009435 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006386 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
